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Volumn 88, Issue , 2015, Pages 60-65

Differential interaction of hGDH1 and hGDH2 with manganese: Implications for metabolism and toxicity

Author keywords

ADP; Glutamate dehydrogenase; hGDH1; hGDH2; Manganese; Mitochondria

Indexed keywords

ADENOSINE DIPHOSPHATE; CALCIUM; DIVALENT CATION; GLUTAMATE DEHYDROGENASE; GLUTAMATE DEHYDROGENASE 1; GLUTAMATE DEHYDROGENASE 2; ISOENZYME; MAGNESIUM; MANGANESE; MITOCHONDRIAL ENZYME; UNCLASSIFIED DRUG; ENZYME INHIBITOR; GLUD1 PROTEIN, HUMAN; GLUD2 PROTEIN, HUMAN; PROTEIN BINDING;

EID: 84939574170     PISSN: 01970186     EISSN: 18729754     Source Type: Journal    
DOI: 10.1016/j.neuint.2015.03.004     Document Type: Article
Times cited : (5)

References (46)
  • 1
    • 24044506991 scopus 로고    scopus 로고
    • Nutritional aspects of manganese homeostasis
    • J.L. Aschner, and M. Aschner Nutritional aspects of manganese homeostasis Mol. Aspects Med 26 2005 353 362
    • (2005) Mol. Aspects Med , vol.26 , pp. 353-362
    • Aschner, J.L.1    Aschner, M.2
  • 2
    • 0026536560 scopus 로고
    • Manganese uptake and efflux in cultured rat astrocytes
    • M. Aschner, M. Gannon, and H.K. Kimelberg Manganese uptake and efflux in cultured rat astrocytes J. Neurochem 58 1992 730 735
    • (1992) J. Neurochem , vol.58 , pp. 730-735
    • Aschner, M.1    Gannon, M.2    Kimelberg, H.K.3
  • 3
    • 72949123199 scopus 로고    scopus 로고
    • Manganese and its role in Parkinson's disease: from transport to neuropathology
    • M. Aschner, K. Erikson, E. Hernández, and R. Tjalkens Manganese and its role in Parkinson's disease: from transport to neuropathology Neuromolecular Med 11 2009 252 266
    • (2009) Neuromolecular Med , vol.11 , pp. 252-266
    • Aschner, M.1    Erikson, K.2    Hernández, E.3    Tjalkens, R.4
  • 4
    • 0020490683 scopus 로고
    • Regulation of bovine glutamate dehydrogenase. The effects of pH and ADP
    • J. Bailey, E.T. Bell, and J.E. Bell Regulation of bovine glutamate dehydrogenase. The effects of pH and ADP J. Biol. Chem 257 1982 5579 5583
    • (1982) J. Biol. Chem , vol.257 , pp. 5579-5583
    • Bailey, J.1    Bell, E.T.2    Bell, J.E.3
  • 5
    • 1542358741 scopus 로고    scopus 로고
    • Manganese potentiates lipopolysaccharide-induced expression of NOS2 in C6 glioma cells through mitochondrial-dependent activation of nuclear factor kappaB
    • R. Barhoumi, J. Faske, Liu X., and R.B. Tjalkens Manganese potentiates lipopolysaccharide-induced expression of NOS2 in C6 glioma cells through mitochondrial-dependent activation of nuclear factor kappaB Molecular Brain Research 122 2004 167 179
    • (2004) Molecular Brain Research , vol.122 , pp. 167-179
    • Barhoumi, R.1    Faske, J.2    Liu, X.3    Tjalkens, R.B.4
  • 6
    • 84895148713 scopus 로고    scopus 로고
    • Considerations on manganese (Mn) treatments for in vitro studies
    • A.B. Bowman, and M. Aschner Considerations on manganese (Mn) treatments for in vitro studies Neurotoxicology 41 2014 141 142
    • (2014) Neurotoxicology , vol.41 , pp. 141-142
    • Bowman, A.B.1    Aschner, M.2
  • 7
    • 0027447043 scopus 로고
    • Manganese injection into the rat striatum produces excitotoxic lesions by impairing energy metabolism
    • E.P. Brouillet, L. Shinobu, U. McGarvey, F. Hochberg, and M.F. Beal Manganese injection into the rat striatum produces excitotoxic lesions by impairing energy metabolism Exp. Neurol 120 1993 89 94
    • (1993) Exp. Neurol , vol.120 , pp. 89-94
    • Brouillet, E.P.1    Shinobu, L.2    McGarvey, U.3    Hochberg, F.4    Beal, M.F.5
  • 8
    • 84906253393 scopus 로고    scopus 로고
    • Genetic factors and manganese-induced neurotoxicity
    • Chen P., N. Parmalee, and M. Aschner Genetic factors and manganese-induced neurotoxicity Front. Gen 5 2014
    • (2014) Front. Gen , vol.5
    • Chen, P.1    Parmalee, N.2    Aschner, M.3
  • 9
    • 34249706788 scopus 로고    scopus 로고
    • Low-level manganese exposure alters glutamate metabolism in GABAergic AF5 cells
    • D.R. Crooks, N. Welch, and D.R. Smith Low-level manganese exposure alters glutamate metabolism in GABAergic AF5 cells Neurotoxicology 28 2007 548 554
    • (2007) Neurotoxicology , vol.28 , pp. 548-554
    • Crooks, D.R.1    Welch, N.2    Smith, D.R.3
  • 11
    • 0025339848 scopus 로고
    • Regulation of glutamate dehydrogenase by Mg2+ and magnification of leucine activation by Mg2+
    • L.A. Fahien, J.K. Teller, M.J. Macdonald, and C.M. Fahien Regulation of glutamate dehydrogenase by Mg2+ and magnification of leucine activation by Mg2+ Mol. Pharmacol 37 1990 943 949
    • (1990) Mol. Pharmacol , vol.37 , pp. 943-949
    • Fahien, L.A.1    Teller, J.K.2    Macdonald, M.J.3    Fahien, C.M.4
  • 12
    • 0017406206 scopus 로고
    • Steady-state kinetics of glutamate dehydrogenase from Pisum sativum L. mitochondria
    • W.J. Garland, and D.T. Dennis Steady-state kinetics of glutamate dehydrogenase from Pisum sativum L. mitochondria Arch. Biochem. Biophys 182 1977 614 625
    • (1977) Arch. Biochem. Biophys , vol.182 , pp. 614-625
    • Garland, W.J.1    Dennis, D.T.2
  • 13
    • 0026611246 scopus 로고
    • Mn2+ sequestration by mitochondria and inhibition of oxidative phosphorylation
    • C.E. Gavin, K.K. Gunter, and T.E. Gunter Mn2+ sequestration by mitochondria and inhibition of oxidative phosphorylation Toxicol. Appl. Pharmacol 115 1992 1 5
    • (1992) Toxicol. Appl. Pharmacol , vol.115 , pp. 1-5
    • Gavin, C.E.1    Gunter, K.K.2    Gunter, T.E.3
  • 14
    • 77957888842 scopus 로고    scopus 로고
    • An analysis of the effects of Mn2+ on oxidative phosphorylation in liver, brain, and heart mitochondria using state 3 oxidation rate assays
    • T.E. Gunter, B. Gerstner, T. Lester, A.P. Wojtovich, J. Malecki, S.G. Swarts, and et al. An analysis of the effects of Mn2+ on oxidative phosphorylation in liver, brain, and heart mitochondria using state 3 oxidation rate assays Toxicol. Appl. Pharmacol 249 2010 65 75
    • (2010) Toxicol. Appl. Pharmacol , vol.249 , pp. 65-75
    • Gunter, T.E.1    Gerstner, B.2    Lester, T.3    Wojtovich, A.P.4    Malecki, J.5    Swarts, S.G.6
  • 15
    • 0030831158 scopus 로고    scopus 로고
    • Manganese decreases glutamate uptake in cultured astrocytes
    • A. Hazell, and M. Norenberg Manganese decreases glutamate uptake in cultured astrocytes Neurochem. Res 22 1997 1443 1447
    • (1997) Neurochem. Res , vol.22 , pp. 1443-1447
    • Hazell, A.1    Norenberg, M.2
  • 18
    • 0027333040 scopus 로고
    • L-glutamate dehydrogenases: distribution, properties and mechanism
    • R. Hudson, and R. Daniel L-glutamate dehydrogenases: distribution, properties and mechanism Comp. Biochem. Physiol. B. 106 1993 767 792
    • (1993) Comp. Biochem. Physiol. B. , vol.106 , pp. 767-792
    • Hudson, R.1    Daniel, R.2
  • 19
    • 0027431229 scopus 로고
    • Glutamate dehydrogenase from the extremely thermophilic archaebacterial isolate AN1
    • R. Hudson, L. Ruttersmith, and R. Daniel Glutamate dehydrogenase from the extremely thermophilic archaebacterial isolate AN1 Biochim. Biophys. Acta 1202 1993 244 250
    • (1993) Biochim. Biophys. Acta , vol.1202 , pp. 244-250
    • Hudson, R.1    Ruttersmith, L.2    Daniel, R.3
  • 20
    • 0018630490 scopus 로고
    • Inhibition of glutamine synthetase activity by manganous ions in a cytosol extract of rat liver
    • S. Joseph, N. Bradford, and J. McGivan Inhibition of glutamine synthetase activity by manganous ions in a cytosol extract of rat liver Biochem. J. 184 1979 477 480
    • (1979) Biochem. J. , vol.184 , pp. 477-480
    • Joseph, S.1    Bradford, N.2    McGivan, J.3
  • 21
    • 0014962945 scopus 로고
    • Superoxide dismutase from Escherichia coli B: a new manganese-containing enzyme
    • B.B. Keele, J.M. McCord, and I. Fridovich Superoxide dismutase from Escherichia coli B: a new manganese-containing enzyme J. Biol. Chem 245 1970 6176 6181
    • (1970) J. Biol. Chem , vol.245 , pp. 6176-6181
    • Keele, B.B.1    McCord, J.M.2    Fridovich, I.3
  • 22
    • 0027934856 scopus 로고
    • Inhibition of glutamate dehydrogenase in brain mitochondria and synaptosomes by Mg2+ and polyamines: a possible cause for its low in vivo activity
    • N. Kuo, M. Michalik, and M. Erecinska Inhibition of glutamate dehydrogenase in brain mitochondria and synaptosomes by Mg2+ and polyamines: a possible cause for its low in vivo activity J. Neurochem 63 1994 751 757
    • (1994) J. Neurochem , vol.63 , pp. 751-757
    • Kuo, N.1    Michalik, M.2    Erecinska, M.3
  • 23
    • 0014670765 scopus 로고
    • Regulation of mitochondrial glutamic dehydrogenase by divalent metals, nucleotides, and α-ketoglutarate: correlations between the molecular and kinetic mechanisms, and the physiological implications
    • H.B. LéJohn, S.G. Jackson, G.R. Klassen, and R.V. Sawula Regulation of mitochondrial glutamic dehydrogenase by divalent metals, nucleotides, and α-ketoglutarate: correlations between the molecular and kinetic mechanisms, and the physiological implications J. Biol. Chem 244 1969 5346 5356
    • (1969) J. Biol. Chem , vol.244 , pp. 5346-5356
    • Léjohn, H.B.1    Jackson, S.G.2    Klassen, G.R.3    Sawula, R.V.4
  • 25
    • 84924599163 scopus 로고    scopus 로고
    • Side-chain interactions in the regulatory domain of human glutamate dehydrogenase determine basal activity and regulation
    • In press
    • V. Mastorodemos, K. Kanavouras, S. Sundaram, M. Providaki, Z. Petraki, M. Kokkinidis, and et al. Side-chain interactions in the regulatory domain of human glutamate dehydrogenase determine basal activity and regulation J. Neurochem 2015 In press
    • (2015) J. Neurochem
    • Mastorodemos, V.1    Kanavouras, K.2    Sundaram, S.3    Providaki, M.4    Petraki, Z.5    Kokkinidis, M.6
  • 26
    • 0014051573 scopus 로고
    • Chronic manganese poisoning. Clinical picture and manganese turnover
    • I. Mena, O. Marin, S. Fuenzalida, and G.C. Cotzias Chronic manganese poisoning. Clinical picture and manganese turnover Neurology 17 1967 128 136
    • (1967) Neurology , vol.17 , pp. 128-136
    • Mena, I.1    Marin, O.2    Fuenzalida, S.3    Cotzias, G.C.4
  • 27
    • 70449720998 scopus 로고    scopus 로고
    • Modeling of ATP-ADP steady-state exchange rate mediated by the adenine nucleotide translocase in isolated mitochondria
    • E. Metelkin, O. Demin, Z. Kovács, and C. Chinopoulos Modeling of ATP-ADP steady-state exchange rate mediated by the adenine nucleotide translocase in isolated mitochondria FEBS J. 276 2009 6942 6955
    • (2009) FEBS J. , vol.276 , pp. 6942-6955
    • Metelkin, E.1    Demin, O.2    Kovács, Z.3    Chinopoulos, C.4
  • 29
    • 79955509072 scopus 로고    scopus 로고
    • Ingestion of Mn and Pb by rats during and after pregnancy alters iron metabolism and behavior in offspring
    • R.M. Molina, S. Phattanarudee, J. Kim, K. Thompson, M. Wessling-Resnick, T.J. Maher, and et al. Ingestion of Mn and Pb by rats during and after pregnancy alters iron metabolism and behavior in offspring Neurotoxicology 32 2011 413 422
    • (2011) Neurotoxicology , vol.32 , pp. 413-422
    • Molina, R.M.1    Phattanarudee, S.2    Kim, J.3    Thompson, K.4    Wessling-Resnick, M.5    Maher, T.J.6
  • 30
    • 0035577286 scopus 로고    scopus 로고
    • Regulation of human glutamate dehydrogenases: implications for glutamate, ammonia and energy metabolism in brain
    • A. Plaitakis, and I. Zaganas Regulation of human glutamate dehydrogenases: implications for glutamate, ammonia and energy metabolism in brain J. Neurosci. Res 66 2001 899 908
    • (2001) J. Neurosci. Res , vol.66 , pp. 899-908
    • Plaitakis, A.1    Zaganas, I.2
  • 32
    • 0028341884 scopus 로고
    • Novel human glutamate dehydrogenase expressed in neural and testicular tissues and encoded by an X-linked intronless gene
    • P. Shashidharan, T.M. Michaelidis, N.K. Robakis, A. Kresovali, J. Papamatheakis, and A. Plaitakis Novel human glutamate dehydrogenase expressed in neural and testicular tissues and encoded by an X-linked intronless gene J. Biol. Chem 269 1994 16971 16976
    • (1994) J. Biol. Chem , vol.269 , pp. 16971-16976
    • Shashidharan, P.1    Michaelidis, T.M.2    Robakis, N.K.3    Kresovali, A.4    Papamatheakis, J.5    Plaitakis, A.6
  • 33
    • 0031003604 scopus 로고    scopus 로고
    • Nerve tissue-specific human glutamate dehydrogenase that is thermolabile and highly regulated by ADP
    • P. Shashidharan, D.D. Clarke, N. Ahmed, N. Moschonas, and A. Plaitakis Nerve tissue-specific human glutamate dehydrogenase that is thermolabile and highly regulated by ADP J. Neurochem 68 1997 1804 1811
    • (1997) J. Neurochem , vol.68 , pp. 1804-1811
    • Shashidharan, P.1    Clarke, D.D.2    Ahmed, N.3    Moschonas, N.4    Plaitakis, A.5
  • 34
    • 84865790575 scopus 로고    scopus 로고
    • The complex regulation of human glud1 and glud2 glutamate dehydrogenases and its implications in nerve tissue biology
    • C. Spanaki, I. Zaganas, Z. Kounoupa, and A. Plaitakis The complex regulation of human glud1 and glud2 glutamate dehydrogenases and its implications in nerve tissue biology Neurochem. Int 61 2012 470 481
    • (2012) Neurochem. Int , vol.61 , pp. 470-481
    • Spanaki, C.1    Zaganas, I.2    Kounoupa, Z.3    Plaitakis, A.4
  • 36
    • 0037222388 scopus 로고    scopus 로고
    • Manganese action in brain function
    • A. Takeda Manganese action in brain function Brain Res. Rev 41 2003 79 87
    • (2003) Brain Res. Rev , vol.41 , pp. 79-87
    • Takeda, A.1
  • 37
    • 0023262306 scopus 로고
    • Chick brain glutamine synthetase and Mn2+-Mg2+ interactions
    • G. Tholey, S. Bloch, M. Ledig, P. Mandel, and F. Wedler Chick brain glutamine synthetase and Mn2+-Mg2+ interactions Neurochem. Res 12 1987 1041 1047
    • (1987) Neurochem. Res , vol.12 , pp. 1041-1047
    • Tholey, G.1    Bloch, S.2    Ledig, M.3    Mandel, P.4    Wedler, F.5
  • 38
    • 0021728238 scopus 로고
    • Glutamine synthetase: the major Mn(II) enzyme in mammalian brain
    • F. Wedler, and R. Denman Glutamine synthetase: the major Mn(II) enzyme in mammalian brain Curr. Top. Cell. Regul 24 1984 153 169
    • (1984) Curr. Top. Cell. Regul , vol.24 , pp. 153-169
    • Wedler, F.1    Denman, R.2
  • 39
    • 0020477024 scopus 로고
    • Glutamine synthetase from ovine brain is a manganese(II) enzyme
    • F. Wedler, R. Denman, and W. Roby Glutamine synthetase from ovine brain is a manganese(II) enzyme Biochemistry 21 1982 6389 6396
    • (1982) Biochemistry , vol.21 , pp. 6389-6396
    • Wedler, F.1    Denman, R.2    Roby, W.3
  • 40
    • 0024785884 scopus 로고
    • Manganese(II) dynamics and distribution in glial cells cultured from chick cerebral cortex
    • F. Wedler, B. Ley, and A. Grippo Manganese(II) dynamics and distribution in glial cells cultured from chick cerebral cortex Neurochem. Res 14 1989 1129 1135
    • (1989) Neurochem. Res , vol.14 , pp. 1129-1135
    • Wedler, F.1    Ley, B.2    Grippo, A.3
  • 41
    • 0014871737 scopus 로고
    • Some aspects of the kinetics of rat liver pyruvate carboxylase
    • J. Wimhurst, and K. Manchester Some aspects of the kinetics of rat liver pyruvate carboxylase Biochem. J. 120 1970 79 93
    • (1970) Biochem. J. , vol.120 , pp. 79-93
    • Wimhurst, J.1    Manchester, K.2
  • 42
    • 0037135619 scopus 로고    scopus 로고
    • Single amino acid substitution (G456A) in the vicinity of the GTP binding domain of human housekeeping glutamate dehydrogenase markedly attenuates GTP inhibition and abolishes the cooperative behavior of the enzyme
    • I. Zaganas, and A. Plaitakis Single amino acid substitution (G456A) in the vicinity of the GTP binding domain of human housekeeping glutamate dehydrogenase markedly attenuates GTP inhibition and abolishes the cooperative behavior of the enzyme J. Biol. Chem 277 2002 26422 26428
    • (2002) J. Biol. Chem , vol.277 , pp. 26422-26428
    • Zaganas, I.1    Plaitakis, A.2
  • 43
    • 0037195942 scopus 로고    scopus 로고
    • Substitution of ser for arg-443 in the regulatory domain of human housekeeping (GLUD1) glutamate dehydrogenase virtually abolishes basal activity and markedly alters the activation of the enzyme by ADP and l-leucine
    • I. Zaganas, C. Spanaki, M. Karpusas, and A. Plaitakis Substitution of ser for arg-443 in the regulatory domain of human housekeeping (GLUD1) glutamate dehydrogenase virtually abolishes basal activity and markedly alters the activation of the enzyme by ADP and l-leucine J. Biol. Chem 277 2002 46552 46558
    • (2002) J. Biol. Chem , vol.277 , pp. 46552-46558
    • Zaganas, I.1    Spanaki, C.2    Karpusas, M.3    Plaitakis, A.4
  • 45
    • 84865755077 scopus 로고    scopus 로고
    • Expression of human GLUD2 glutamate dehydrogenase in human tissues: functional implications
    • I. Zaganas, C. Spanaki, and A. Plaitakis Expression of human GLUD2 glutamate dehydrogenase in human tissues: functional implications Neurochem. Int 61 2012 455 462
    • (2012) Neurochem. Int , vol.61 , pp. 455-462
    • Zaganas, I.1    Spanaki, C.2    Plaitakis, A.3
  • 46
    • 0038457946 scopus 로고    scopus 로고
    • Energy metabolism in astrocytes and neurons treated with manganese; relation among cell-specific energy failure, glucose metabolism, and intercellular trafficking using multinuclear NMR-spectroscopic analysis
    • C. Zwingmann, D. Leibfritz, and A.S. Hazell Energy metabolism in astrocytes and neurons treated with manganese; relation among cell-specific energy failure, glucose metabolism, and intercellular trafficking using multinuclear NMR-spectroscopic analysis J. Cereb. Blood Flow Metab 23 2003 756 771
    • (2003) J. Cereb. Blood Flow Metab , vol.23 , pp. 756-771
    • Zwingmann, C.1    Leibfritz, D.2    Hazell, A.S.3


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